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1 The characteristics of the binding of 12‐alpha‐[3H]‐digoxin to the membranes of intact human erythrocytes are described. 2 Only one class of binding site can be demonstrated. Binding is time‐ and temperature‐ dependent, saturable and slowly reversible; it is inhibited by other cardiac glycosides and by potassium. 3 Pre‐incubation with unlabelled digoxin reduces the subsequent binding of 12‐alpha‐[3H]‐digoxin in stoichiometric fashion. 4 The possible application of the measurement of the binding of 12‐alpha‐[3H]‐digoxin to the study of biochemical pharmacological events occurring during digoxin therapy is discussed. 1979 The British Pharmacological Society

Original publication




Journal article


British Journal of Clinical Pharmacology

Publication Date





115 - 124